1jqn

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[[Image:1jqn.gif|left|200px]]<br /><applet load="1jqn" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1jqn, resolution 2.35&Aring;" />
 
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'''Crystal structure of E.coli phosphoenolpyruvate carboxylase in complex with Mn2+ and DCDP'''<br />
 
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==Overview==
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==Crystal structure of E.coli phosphoenolpyruvate carboxylase in complex with Mn2+ and DCDP==
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Phosphoenolpyruvate carboxylase (PEPC) catalyzes the first step in the fixation of atmospheric CO(2) during C(4) photosynthesis. The crystal structure of C(4) form maize PEPC (ZmPEPC), the first structure of the plant PEPCs, has been determined at 3.0 A resolution. The structure includes a sulfate ion at the plausible binding site of an allosteric activator, glucose 6-phosphate. The crystal structure of E. coli PEPC (EcPEPC) complexed with Mn(2+), phosphoenolpyruvate analog (3,3-dichloro-2-dihydroxyphosphinoylmethyl-2-propenoate), and an allosteric inhibitor, aspartate, has also been determined at 2.35 A resolution. Dynamic movements were found in the ZmPEPC structure, compared with the EcPEPC structure, around two loops near the active site. On the basis of these molecular structures, the mechanisms for the carboxylation reaction and for the allosteric regulation of PEPC are proposed.
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<StructureSection load='1jqn' size='340' side='right'caption='[[1jqn]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1jqn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JQN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JQN FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=DCO:3,3-DICHLORO-2-PHOSPHONOMETHYL-ACRYLIC+ACID'>DCO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jqn OCA], [https://pdbe.org/1jqn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jqn RCSB], [https://www.ebi.ac.uk/pdbsum/1jqn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jqn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAPP_ECOLI CAPP_ECOLI] Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.[HAMAP-Rule:MF_00595]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jq/1jqn_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jqn ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1JQN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=ASP:'>ASP</scene> and <scene name='pdbligand=DCO:'>DCO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxylase Phosphoenolpyruvate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.31 4.1.1.31] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JQN OCA].
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*[[Phosphoenolpyruvate carboxylase|Phosphoenolpyruvate carboxylase]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structures of C4 form maize and quaternary complex of E. coli phosphoenolpyruvate carboxylases., Matsumura H, Xie Y, Shirakata S, Inoue T, Yoshinaga T, Ueno Y, Izui K, Kai Y, Structure. 2002 Dec;10(12):1721-30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12467579 12467579]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Phosphoenolpyruvate carboxylase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Kai Y]]
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[[Category: Kai, Y.]]
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[[Category: Matsumura H]]
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[[Category: Matsumura, H.]]
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[[Category: ASP]]
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[[Category: DCO]]
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[[Category: MN]]
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[[Category: beta barrel]]
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[[Category: mn2+ and dcdp complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:37 2008''
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Current revision

Crystal structure of E.coli phosphoenolpyruvate carboxylase in complex with Mn2+ and DCDP

PDB ID 1jqn

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